6md4

Crystal Structure of Human PPARgamma Ligand Binding Domain in Complex with Rosiglitazone and Oleic acid

Method: X-RAY DIFFRACTION Dmax: 84.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Peroxisome proliferator-activated receptor gamma

Homo sapiens

UniProt P37231

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 231–505 Not recorded BRL 2,4-THIAZOLIDIINEDIONE, 5-[[4-[2-(METHYL-2-PYRIDINYLAMINO)ETHOXY]PHENYL]METHYL]-(9CL) × 1 OLA OLEIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;293 K;0.1M MOPS, pH 7.4 0.8M SODIUM CITRATE Resolution 2.24 Å R-free 0.282
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 231–505 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;293 K;0.1M MOPS, pH 7.4 0.8M SODIUM CITRATE Resolution 2.24 Å R-free 0.282

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

369 other PDB entries and 499 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPARG_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–275; UniProt 231–505 Author chain B; PDBConstruct 1–275; UniProt 231–505

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6md4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6md4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6md4
Deposition date deposition_date2018-09-03
Structure title titleCrystal Structure of Human PPARgamma Ligand Binding Domain in Complex with Rosiglitazone and Oleic acid
Keywords keywordsNuclear receptors, TZDs, Drug design, Therapeutic targets, transcription-transcription inhibitor complex; transcription/transcription inhibitor
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.07
Radius of gyration Rg (electron density) rg_electron25.08
Forward intensity I(0) i050067200.00
Molecular weight molecular_weight58631.0 kDa
Excluded volume excluded_volume75090 ų
Envelope volume envelope_volume90514 ų
Hydration-shell volume shell_volume29868 ų
Envelope diameter envelope_diameter86.9
Shell Rg shell_rg32.40
Envelope Rg envelope_rg25.17
Shape Rg shape_rg25.05
Total Rg total_rg26.06
Total atoms total_atoms4126
Residues n_residues509
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax84.7
Rg (real space) rg_real26.01
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real5.0070e+07
I(0) uncertainty (real space) i0_real_error6.8090e+05
Rg (reciprocal space) rg_reciprocal26.03
I(0) (reciprocal space) i0_reciprocal50070000.0000
Solution quality estimate total_estimate0.8886
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14070000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.904

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6md4a_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain
Domain ID domain_idd6md4b_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id6md4A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id6md4B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor

8. Citations (1)

9. Files and Curves (10)